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A more recent version of this article appeared on September 1, 2003

Papers In Press, published online ahead of print June 16, 2003
J. Lipid Res., doi:10.1194/jlr.M300018-JLR200
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Submitted on January 13, 2003
Revised on May 28, 2003
Accepted on June 5, 2003

Calcium-independent phospholipase A2 mediates CREB phosphorylation in double-stranded RNA-stimulated endothelial cells

Bradley D. Martinson, Carolyn J. Albert, John A. Corbett, Robert B. Wysolmerski, and David A. Ford

Department of Biochemistry, Saint Louis University, St. Louis, MO 63104

Corresponding Author: fordda{at}slu.edu

One of the products of calcium-independent phospholipase A2 (iPLA2) attack of plasmenylcholine, lysoplasmenylcholine, has previously been shown to activate cAMP-dependent protein kinase (PKA). Since endothelial cells respond to some agonists in part by the activation of iPLA2, the present study was designed to determine whether double-stranded RNA, the primary activator of the antiviral response in endothelial cells, elicits cAMP response element binding protein (CREB) phosphorylation through a mechanism mediated by iPLA2. Double stranded RNA stimulated CREB phosphorylation in bovine pulmonary artery endothelial cells that was inhibited by the iPLA2 inhibitor, bromoenol lactone, and the PKA inhibitor, H-89. Additionally, the product of iPLA2 hydrolysis of plasmenylcholine, lysoplasmenylcholine, elicited CREB phosphorylation in bovine pulmonary endothelial cells. Taken together the present studies suggest that double-stranded RNA as well as other agonists of endothelial cells elicit signaling mechanisms that include in part CREB phosphorylation mediated by iPLA2.


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